SCOPe 2.08: Domain d1il2a3: 1il2 A:107-287,A:421-585

Lineage for d1il2a3 (1il2 A:107-287,A:421-585)

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 folds)

3. Fold d.104: Class II aaRS and biotin synthetases [55680] (1 superfamily)
   contains large mixed beta-sheet

4. Superfamily d.104.1: Class II aaRS and biotin synthetases [55681] (5 families)

5. Family d.104.1.1: Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain [55682] (16 proteins)

6. Protein Aspartyl-tRNA synthetase (AspRS) [55696] (5 species)

7. Species Escherichia coli [TaxId:562] [55699] (3 PDB entries)

8. Domain d1il2a3: 1il2 A:107-287,A:421-585 [66195]
   Other proteins in same PDB: d1il2a1, d1il2a2, d1il2b1, d1il2b2
   protein/RNA complex; complexed with amo, so4
   has additional insertions and/or extensions that are not grouped together

Details for d1il2a3

PDB Entry: 1il2, 2.6 Å

PDB Description: crystal structure of the e. coli aspartyl-trna synthetase:yeast trnaasp:aspartyl-adenylate complex

PDB Compounds: (A:) ASPARTYL-tRNA SYNTHETASE

SCOPe Domain Sequences for d1il2a3:

Sequence; same for both SEQRES and ATOM records:

>d1il2a3 d.104.1.1 (A:107-287,A:421-585) Aspartyl-tRNA synthetase (AspRS) {Escherichia coli [TaxId: 562]}
vlpldsnhvnteearlkyryldlrrpemaqrlktrakitslvrrfmddhgfldietpmlt
katpegardylvpsrvhkgkfyalpqspqlfkqllmmsgfdryyqivkcfrdedlradrq
peftqidvetsfmtapqvrevmealvrhlwlevkgvdlgdfpvmtfaeaerrygsdkpdl
rXdeskwaplwvidfpmfeddgeggltamhhpftspkdmtaaelkaapenavanaydmvi
ngyevgggsvrihngdmqqtvfgilgineeeqrekfgflldalkygtpphaglafgldrl
tmlltgtdnirdviafpkttaaaclmteapsfanptalaelsiqvvk

Timeline for d1il2a3:

• d1il2a3 first appeared in SCOP 1.59
  
• d1il2a3 appears in SCOPe 2.07